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Entry version 129 (08 May 2019)
Sequence version 1 (01 Jun 2003)
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Protein

Inositol monophosphatase 3

Gene

Impad1

Organism
Mus musculus (Mouse)
Status
Reviewed-Annotation score:

Annotation score:5 out of 5

<p>The annotation score provides a heuristic measure of the annotation content of a UniProtKB entry or proteome. This score <strong>cannot</strong> be used as a measure of the accuracy of the annotation as we cannot define the ‘correct annotation’ for any given protein.<p><a href='/help/annotation_score' target='_top'>More...</a></p>
-Experimental evidence at protein leveli <p>This indicates the type of evidence that supports the existence of the protein. Note that the ‘protein existence’ evidence does not give information on the accuracy or correctness of the sequence(s) displayed.<p><a href='/help/protein_existence' target='_top'>More...</a></p>

<p>This section provides any useful information about the protein, mostly biological knowledge.<p><a href='/help/function_section' target='_top'>More...</a></p>Functioni

May play a role in the formation of skeletal elements derived through endochondral ossification, possibly by clearing adenosine 3',5'-bisphosphate produced by Golgi sulfotransferases during glycosaminoglycan sulfation.1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the catalytic activity of an enzyme, i.e. a chemical reaction that the enzyme catalyzes.<p><a href='/help/catalytic_activity' target='_top'>More...</a></p>Catalytic activityi

<p>This subsection of the ‘Function’ section provides information relevant to cofactors. A cofactor is any non-protein substance required for a protein to be catalytically active. Some cofactors are inorganic, such as the metal atoms zinc, iron, and copper in various oxidation states. Others, such as most vitamins, are organic.<p><a href='/help/cofactor' target='_top'>More...</a></p>Cofactori

Mg2+By similarity

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes regulatory mechanisms for enzymes, transporters or microbial transcription factors, and reports the components which regulate (by activation or inhibition) the reaction.<p><a href='/help/activity_regulation' target='_top'>More...</a></p>Activity regulationi

Strongly inhibited by lithium.1 Publication

<p>This subsection of the ‘Function’ section describes biophysical and chemical properties, such as maximal absorption, kinetic parameters, pH dependence, redox potentials and temperature dependence.<p><a href='/help/biophysicochemical_properties' target='_top'>More...</a></p>Kineticsi

  1. KM=21 µM for 3'-phosphoadenosine 5'- phosphate (PAP)1 Publication
  1. Vmax=9.5 µmol/min/mg enzyme1 Publication

<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">'Function'</a> section describes the metabolic pathway(s) associated with a protein.<p><a href='/help/pathway' target='_top'>More...</a></p>Pathwayi: myo-inositol biosynthesis

This protein is involved in step 2 of the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate.
Proteins known to be involved in the 2 steps of the subpathway in this organism are:
  1. Inositol-3-phosphate synthase 1 (Isyna1)
  2. Inositol-1-monophosphatase (Impa1), Inositol-1-monophosphatase (Impa1), Inositol-1-monophosphatase (Impa1), Inositol-1-monophosphatase (Impa1), Inositol-1-monophosphatase (Impa1), Inositol monophosphatase 1 (Impa1), Inositol-1-monophosphatase (Impa2), Inositol monophosphatase 2 (Impa2), Inositol monophosphatase 3 (Impad1), Inositol-1-monophosphatase (Impa2), Inositol-1-monophosphatase (Impa2), Inositol-1-monophosphatase (Impa1), Inositol-1-monophosphatase (Impa2)
This subpathway is part of the pathway myo-inositol biosynthesis, which is itself part of Polyol metabolism.
View all proteins of this organism that are known to be involved in the subpathway that synthesizes myo-inositol from D-glucose 6-phosphate, the pathway myo-inositol biosynthesis and in Polyol metabolism.

Sites

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section indicates at which position the protein binds a given metal ion. The nature of the metal is indicated in the ‘Description’ field.<p><a href='/help/metal' target='_top'>More...</a></p>Metal bindingi131Magnesium 1By similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/function_section">Function</a> section describes the interaction between a single amino acid and another chemical entity. Priority is given to the annotation of physiological ligands.<p><a href='/help/binding' target='_top'>More...</a></p>Binding sitei131SubstrateBy similarity1
Metal bindingi172Magnesium 1By similarity1
Metal bindingi172Magnesium 2By similarity1
Metal bindingi174Magnesium 1; via carbonyl oxygenBy similarity1
Metal bindingi175Magnesium 2By similarity1
Metal bindingi298Magnesium 2By similarity1
Binding sitei298SubstrateBy similarity1

<p>The <a href="http://www.geneontology.org/">Gene Ontology (GO)</a> project provides a set of hierarchical controlled vocabulary split into 3 categories:<p><a href='/help/gene_ontology' target='_top'>More...</a></p>GO - Molecular functioni

GO - Biological processi

<p>UniProtKB Keywords constitute a <a href="http://www.uniprot.org/keywords">controlled vocabulary</a> with a hierarchical structure. Keywords summarise the content of a UniProtKB entry and facilitate the search for proteins of interest.<p><a href='/help/keywords' target='_top'>More...</a></p>Keywordsi

Molecular functionHydrolase
LigandMagnesium, Metal-binding

Enzyme and pathway databases

BRENDA Comprehensive Enzyme Information System

More...
BRENDAi
3.1.3.7 3474

Reactome - a knowledgebase of biological pathways and processes

More...
Reactomei
R-MMU-156584 Cytosolic sulfonation of small molecules

UniPathway: a resource for the exploration and annotation of metabolic pathways

More...
UniPathwayi
UPA00823;UER00788

<p>This section provides information about the protein and gene name(s) and synonym(s) and about the organism that is the source of the protein sequence.<p><a href='/help/names_and_taxonomy_section' target='_top'>More...</a></p>Names & Taxonomyi

<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides an exhaustive list of all names of the protein, from commonly used to obsolete, to allow unambiguous identification of a protein.<p><a href='/help/protein_names' target='_top'>More...</a></p>Protein namesi
Recommended name:
Inositol monophosphatase 3 (EC:3.1.3.25, EC:3.1.3.7)
Short name:
IMP 3
Short name:
IMPase 3
Alternative name(s):
Golgi 3-prime phosphoadenosine 5-prime phosphate 3-prime phosphatase
Short name:
Golgi-resident PAP phosphatase
Short name:
gPAPP
Inositol monophosphatase domain-containing protein 1
Inositol-1(or 4)-monophosphatase 3
Myo-inositol monophosphatase A3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section indicates the name(s) of the gene(s) that code for the protein sequence(s) described in the entry. Four distinct tokens exist: ‘Name’, ‘Synonyms’, ‘Ordered locus names’ and ‘ORF names’.<p><a href='/help/gene_name' target='_top'>More...</a></p>Gene namesi
Name:Impad1
Synonyms:Impa3
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section provides information on the name(s) of the organism that is the source of the protein sequence.<p><a href='/help/organism-name' target='_top'>More...</a></p>OrganismiMus musculus (Mouse)
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section shows the unique identifier assigned by the NCBI to the source organism of the protein. This is known as the ‘taxonomic identifier’ or ‘taxid’.<p><a href='/help/taxonomic_identifier' target='_top'>More...</a></p>Taxonomic identifieri10090 [NCBI]
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section contains the taxonomic hierarchical classification lineage of the source organism. It lists the nodes as they appear top-down in the taxonomic tree, with the more general grouping listed first.<p><a href='/help/taxonomic_lineage' target='_top'>More...</a></p>Taxonomic lineageiEukaryotaMetazoaChordataCraniataVertebrataEuteleostomiMammaliaEutheriaEuarchontogliresGliresRodentiaMyomorphaMuroideaMuridaeMurinaeMusMus
<p>This subsection of the <a href="http://www.uniprot.org/help/names_and_taxonomy_section">Names and taxonomy</a> section is present for entries that are part of a <a href="http://www.uniprot.org/proteomes">proteome</a>, i.e. of a set of proteins thought to be expressed by organisms whose genomes have been completely sequenced.<p><a href='/help/proteomes_manual' target='_top'>More...</a></p>Proteomesi
  • UP000000589 <p>A UniProt <a href="http://www.uniprot.org/manual/proteomes_manual">proteome</a> can consist of several components. <br></br>The component name refers to the genomic component encoding a set of proteins.<p><a href='/help/proteome_component' target='_top'>More...</a></p> Componenti: Chromosome 4

Organism-specific databases

Mouse genome database (MGD) from Mouse Genome Informatics (MGI)

More...
MGIi
MGI:1915720 Impad1

<p>This section provides information on the location and the topology of the mature protein in the cell.<p><a href='/help/subcellular_location_section' target='_top'>More...</a></p>Subcellular locationi

Extracellular region or secreted Cytosol Plasma membrane Cytoskeleton Lysosome Endosome Peroxisome ER Golgi apparatus Nucleus Mitochondrion Manual annotation Automatic computational assertionGraphics by Christian Stolte & Seán O’Donoghue; Source: COMPARTMENTS

Topology

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the subcellular compartment where each non-membrane region of a membrane-spanning protein is found.<p><a href='/help/topo_dom' target='_top'>More...</a></p>Topological domaini1 – 12CytoplasmicSequence analysisAdd BLAST12
<p>This subsection of the <a href="http://www.uniprot.org/help/subcellular_location_section">'Subcellular location'</a> section describes the extent of a membrane-spanning region of the protein. It denotes the presence of both alpha-helical transmembrane regions and the membrane spanning regions of beta-barrel transmembrane proteins.<p><a href='/help/transmem' target='_top'>More...</a></p>Transmembranei13 – 33HelicalSequence analysisAdd BLAST21
Topological domaini34 – 356LumenalSequence analysisAdd BLAST323

Keywords - Cellular componenti

Golgi apparatus, Membrane

<p>This section provides information on the disease(s) and phenotype(s) associated with a protein.<p><a href='/help/pathology_and_biotech_section' target='_top'>More...</a></p>Pathology & Biotechi

<p>This subsection of the ‘Pathology and Biotech’ section describes the in vivo effects caused by ablation of the gene (or one or more transcripts) coding for the protein described in the entry. This includes gene knockout and knockdown, provided experiments have been performed in the context of a whole organism or a specific tissue, and not at the single-cell level.<p><a href='/help/disruption_phenotype' target='_top'>More...</a></p>Disruption phenotypei

Mutant animals experience severe respiratory distress and died within minutes after birth. At 18.5 dpc, lungs exhibit small alveolar spaces and thickened septa. The rib cage cartilage is hypocellular with abnormal, fibrous-appearing extracellular matrix. Animals show severe skeletal abnormalities, most notably in the longitudinal growth of bones formed by endochondral ossification. The length of the axial skeleton is reduced. The appendicular bones of the upper limbs, as well as the ilium, femur, tibia and fibula of the lower limbs are markedly shorter than in wild-type littermates. The rib cages display malformation characterized by reduced sternal length and correspondingly diminished rib spacing. The process of intramembranous ossification is normal. Mutant animals exhibit a deficiency in glycosaminoglycan sulfation. Mutant cartilage and lung exhibit a substantial decrease in chondroitin 4-sulfate and an increase in nonsulfated chondroitin compared with wild type tissue.1 Publication

<p>This section describes post-translational modifications (PTMs) and/or processing events.<p><a href='/help/ptm_processing_section' target='_top'>More...</a></p>PTM / Processingi

Molecule processing

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section describes the extent of a polypeptide chain in the mature protein following processing.<p><a href='/help/chain' target='_top'>More...</a></p>ChainiPRO_00002890421 – 356Inositol monophosphatase 3Add BLAST356

Amino acid modifications

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘PTM / Processing’ section specifies the position and type of each modified residue excluding <a href="http://www.uniprot.org/manual/lipid">lipids</a>, <a href="http://www.uniprot.org/manual/carbohyd">glycans</a> and <a href="http://www.uniprot.org/manual/crosslnk">protein cross-links</a>.<p><a href='/help/mod_res' target='_top'>More...</a></p>Modified residuei1N-acetylmethionineBy similarity1
<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM / Processing</a> section specifies the position and type of each covalently attached glycan group (mono-, di-, or polysaccharide).<p><a href='/help/carbohyd' target='_top'>More...</a></p>Glycosylationi257N-linked (GlcNAc...) asparagineSequence analysis1

<p>This subsection of the <a href="http://www.uniprot.org/help/ptm_processing_section">PTM/processing</a> section describes post-translational modifications (PTMs). This subsection <strong>complements</strong> the information provided at the sequence level or describes modifications for which <strong>position-specific data is not yet available</strong>.<p><a href='/help/post-translational_modification' target='_top'>More...</a></p>Post-translational modificationi

Contains N-linked glycan resistant to endoglycosydase H.By similarity

Keywords - PTMi

Acetylation, Glycoprotein

Proteomic databases

Encyclopedia of Proteome Dynamics

More...
EPDi
Q80V26

jPOST - Japan Proteome Standard Repository/Database

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jPOSTi
Q80V26

MaxQB - The MaxQuant DataBase

More...
MaxQBi
Q80V26

PaxDb, a database of protein abundance averages across all three domains of life

More...
PaxDbi
Q80V26

PeptideAtlas

More...
PeptideAtlasi
Q80V26

PRoteomics IDEntifications database

More...
PRIDEi
Q80V26

Consortium for Top Down Proteomics

More...
TopDownProteomicsi
Q80V26

PTM databases

Comprehensive resource for the study of protein post-translational modifications (PTMs) in human, mouse and rat.

More...
PhosphoSitePlusi
Q80V26

SwissPalm database of S-palmitoylation events

More...
SwissPalmi
Q80V26

<p>This section provides information on the expression of a gene at the mRNA or protein level in cells or in tissues of multicellular organisms.<p><a href='/help/expression_section' target='_top'>More...</a></p>Expressioni

<p>This subsection of the ‘Expression’ section provides information on the expression of the gene product at various stages of a cell, tissue or organism development. By default, the information is derived from experiments at the mRNA level, unless specified ‘at the protein level’.<p><a href='/help/developmental_stage' target='_top'>More...</a></p>Developmental stagei

At 18.5 dpc, widely expressed with enhanced levels in brain, spinal cord, lung and kidney, including medulla and cortex. In the developing brain, strongly expressed in the neopallial cortex and throughout the cerebellum with intense expression within the developing Purkinje cells and adjacent choroid plexus. Strong expression also observed within the pons and throughout the medulla oblongata. In the lung, expressed in individual pneumocytes and particularly in cells surrounding developing bronchi/bronchioles. Moderate expression in chondrocytes of costal cartilage and in the surrounding perichondrium.1 Publication

Gene expression databases

Bgee dataBase for Gene Expression Evolution

More...
Bgeei
ENSMUSG00000066324 Expressed in 287 organ(s), highest expression level in rostral migratory stream

Genevisible search portal to normalized and curated expression data from Genevestigator

More...
Genevisiblei
Q80V26 MM

<p>This section provides information on the quaternary structure of a protein and on interaction(s) with other proteins or protein complexes.<p><a href='/help/interaction_section' target='_top'>More...</a></p>Interactioni

Protein-protein interaction databases

The Biological General Repository for Interaction Datasets (BioGrid)

More...
BioGridi
232391, 1 interactor

STRING: functional protein association networks

More...
STRINGi
10090.ENSMUSP00000082013

<p>This section provides information on the tertiary and secondary structure of a protein.<p><a href='/help/structure_section' target='_top'>More...</a></p>Structurei

3D structure databases

SWISS-MODEL Repository - a database of annotated 3D protein structure models

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SMRi
Q80V26

Database of comparative protein structure models

More...
ModBasei
Search...

<p>This section provides information on sequence similarities with other proteins and the domain(s) present in a protein.<p><a href='/help/family_and_domains_section' target='_top'>More...</a></p>Family & Domainsi

Region

Feature keyPosition(s)DescriptionActionsGraphical viewLength
<p>This subsection of the ‘Family and Domains’ section describes a region of interest that cannot be described in other subsections.<p><a href='/help/region' target='_top'>More...</a></p>Regioni174 – 177Substrate bindingBy similarity4

<p>This subsection of the ‘Family and domains’ section provides information about the sequence similarity with other proteins.<p><a href='/help/sequence_similarities' target='_top'>More...</a></p>Sequence similaritiesi

Keywords - Domaini

Signal-anchor, Transmembrane, Transmembrane helix

Phylogenomic databases

evolutionary genealogy of genes: Non-supervised Orthologous Groups

More...
eggNOGi
KOG3853 Eukaryota
COG1218 LUCA

Ensembl GeneTree

More...
GeneTreei
ENSGT00940000160216

The HOGENOM Database of Homologous Genes from Fully Sequenced Organisms

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HOGENOMi
HOG000290671

InParanoid: Eukaryotic Ortholog Groups

More...
InParanoidi
Q80V26

KEGG Orthology (KO)

More...
KOi
K15759

Identification of Orthologs from Complete Genome Data

More...
OMAi
GQTAWAW

Database of Orthologous Groups

More...
OrthoDBi
1096950at2759

Database for complete collections of gene phylogenies

More...
PhylomeDBi
Q80V26

TreeFam database of animal gene trees

More...
TreeFami
TF314300

Family and domain databases

Integrated resource of protein families, domains and functional sites

More...
InterProi
View protein in InterPro
IPR000760 Inositol_monophosphatase-like
IPR020550 Inositol_monophosphatase_CS

Pfam protein domain database

More...
Pfami
View protein in Pfam
PF00459 Inositol_P, 1 hit

PROSITE; a protein domain and family database

More...
PROSITEi
View protein in PROSITE
PS00630 IMP_2, 1 hit

<p>This section displays by default the canonical protein sequence and upon request all isoforms described in the entry. It also includes information pertinent to the sequence(s), including <a href="http://www.uniprot.org/help/sequence_length">length</a> and <a href="http://www.uniprot.org/help/sequences">molecular weight</a>. The information is filed in different subsections. The current subsections and their content are listed below:<p><a href='/help/sequences_section' target='_top'>More...</a></p>Sequencei

<p>This subsection of the <a href="http://www.uniprot.org/help/sequences_section">Sequence</a> section indicates if the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> displayed by default in the entry is complete or not.<p><a href='/help/sequence_status' target='_top'>More...</a></p>Sequence statusi: Complete.

Q80V26-1 [UniParc]FASTAAdd to basket
« Hide
        10         20         30         40         50
MAPMGIRLSP LGVAVFFLLG LGVLYHLYSG FLAGRFSLFG LGSEPAAGEA
60 70 80 90 100
EVASDGGTVD LREMLAVAVL AAERGGDEVR RVRESNVLHE KSKGKTREGA
110 120 130 140 150
DDKMTSGDVL SNRKMFYLLK TAFPNVQINT EEHVDASDKE VIVWNRKIPE
160 170 180 190 200
DILKEIAAPK EVPAESVTVW IDPLDATQEY TEDLRKYVTT MVCVAVNGKP
210 220 230 240 250
VLGVIHKPFS EYTAWAMVDG GSNVKARSSY NEKTPKIIVS RSHAGMVKQV
260 270 280 290 300
ALQTFGNQTS IIPAGGAGYK VLALLDVPDM TQEKADLYIH VTYIKKWDIC
310 320 330 340 350
AGNAILKALG GHMTTLNGEE ISYTGSDGIE GGLLASIRMN HQALVRKLPD

LEKSGH
Length:356
Mass (Da):38,616
Last modified:June 1, 2003 - v1
<p>The checksum is a form of redundancy check that is calculated from the sequence. It is useful for tracking sequence updates.</p> <p>It should be noted that while, in theory, two different sequences could have the same checksum value, the likelihood that this would happen is extremely low.</p> <p>However UniProtKB may contain entries with identical sequences in case of multiple genes (paralogs).</p> <p>The checksum is computed as the sequence 64-bit Cyclic Redundancy Check value (CRC64) using the generator polynomial: x<sup>64</sup> + x<sup>4</sup> + x<sup>3</sup> + x + 1. The algorithm is described in the ISO 3309 standard. </p> <p class="publication">Press W.H., Flannery B.P., Teukolsky S.A. and Vetterling W.T.<br /> <strong>Cyclic redundancy and other checksums</strong><br /> <a href="http://www.nrbook.com/b/bookcpdf.php">Numerical recipes in C 2nd ed., pp896-902, Cambridge University Press (1993)</a>)</p> Checksum:iF01BF0082F5C7C82
GO

Sequence databases

Select the link destinations:

EMBL nucleotide sequence database

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EMBLi

GenBank nucleotide sequence database

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GenBanki

DNA Data Bank of Japan; a nucleotide sequence database

More...
DDBJi
Links Updated
AL772346 Genomic DNA No translation available.
CH466538 Genomic DNA Translation: EDL05698.1
BC048776 mRNA Translation: AAH48776.1
BC138209 mRNA Translation: AAI38210.1
BC145952 mRNA Translation: AAI45953.1

The Consensus CDS (CCDS) project

More...
CCDSi
CCDS17947.1

NCBI Reference Sequences

More...
RefSeqi
NP_808398.1, NM_177730.3

Genome annotation databases

Ensembl eukaryotic genome annotation project

More...
Ensembli
ENSMUST00000084949; ENSMUSP00000082013; ENSMUSG00000066324

Database of genes from NCBI RefSeq genomes

More...
GeneIDi
242291

KEGG: Kyoto Encyclopedia of Genes and Genomes

More...
KEGGi
mmu:242291

UCSC genome browser

More...
UCSCi
uc008rxc.2 mouse

<p>This section provides links to proteins that are similar to the protein sequence(s) described in this entry at different levels of sequence identity thresholds (100%, 90% and 50%) based on their membership in UniProt Reference Clusters (<a href="http://www.uniprot.org/help/uniref">UniRef</a>).<p><a href='/help/similar_proteins_section' target='_top'>More...</a></p>Similar proteinsi

<p>This section is used to point to information related to entries and found in data collections other than UniProtKB.<p><a href='/help/cross_references_section' target='_top'>More...</a></p>Cross-referencesi

Sequence databases

Select the link destinations:
EMBLi
GenBanki
DDBJi
Links Updated
AL772346 Genomic DNA No translation available.
CH466538 Genomic DNA Translation: EDL05698.1
BC048776 mRNA Translation: AAH48776.1
BC138209 mRNA Translation: AAI38210.1
BC145952 mRNA Translation: AAI45953.1
CCDSiCCDS17947.1
RefSeqiNP_808398.1, NM_177730.3

3D structure databases

SMRiQ80V26
ModBaseiSearch...

Protein-protein interaction databases

BioGridi232391, 1 interactor
STRINGi10090.ENSMUSP00000082013

PTM databases

PhosphoSitePlusiQ80V26
SwissPalmiQ80V26

Proteomic databases

EPDiQ80V26
jPOSTiQ80V26
MaxQBiQ80V26
PaxDbiQ80V26
PeptideAtlasiQ80V26
PRIDEiQ80V26
TopDownProteomicsiQ80V26

Protocols and materials databases

Structural Biology KnowledgebaseSearch...

Genome annotation databases

EnsembliENSMUST00000084949; ENSMUSP00000082013; ENSMUSG00000066324
GeneIDi242291
KEGGimmu:242291
UCSCiuc008rxc.2 mouse

Organism-specific databases

Comparative Toxicogenomics Database

More...
CTDi
54928
MGIiMGI:1915720 Impad1

Phylogenomic databases

eggNOGiKOG3853 Eukaryota
COG1218 LUCA
GeneTreeiENSGT00940000160216
HOGENOMiHOG000290671
InParanoidiQ80V26
KOiK15759
OMAiGQTAWAW
OrthoDBi1096950at2759
PhylomeDBiQ80V26
TreeFamiTF314300

Enzyme and pathway databases

UniPathwayiUPA00823;UER00788
BRENDAi3.1.3.7 3474
ReactomeiR-MMU-156584 Cytosolic sulfonation of small molecules

Miscellaneous databases

ChiTaRS: a database of human, mouse and fruit fly chimeric transcripts and RNA-sequencing data

More...
ChiTaRSi
Impad1 mouse

Protein Ontology

More...
PROi
PR:Q80V26

The Stanford Online Universal Resource for Clones and ESTs

More...
SOURCEi
Search...

Gene expression databases

BgeeiENSMUSG00000066324 Expressed in 287 organ(s), highest expression level in rostral migratory stream
GenevisibleiQ80V26 MM

Family and domain databases

InterProiView protein in InterPro
IPR000760 Inositol_monophosphatase-like
IPR020550 Inositol_monophosphatase_CS
PfamiView protein in Pfam
PF00459 Inositol_P, 1 hit
PROSITEiView protein in PROSITE
PS00630 IMP_2, 1 hit

ProtoNet; Automatic hierarchical classification of proteins

More...
ProtoNeti
Search...

MobiDB: a database of protein disorder and mobility annotations

More...
MobiDBi
Search...

<p>This section provides general information on the entry.<p><a href='/help/entry_information_section' target='_top'>More...</a></p>Entry informationi

<p>This subsection of the ‘Entry information’ section provides a mnemonic identifier for a UniProtKB entry, but it is not a stable identifier. Each reviewed entry is assigned a unique entry name upon integration into UniProtKB/Swiss-Prot.<p><a href='/help/entry_name' target='_top'>More...</a></p>Entry nameiIMPA3_MOUSE
<p>This subsection of the ‘Entry information’ section provides one or more accession number(s). These are stable identifiers and should be used to cite UniProtKB entries. Upon integration into UniProtKB, each entry is assigned a unique accession number, which is called ‘Primary (citable) accession number’.<p><a href='/help/accession_numbers' target='_top'>More...</a></p>AccessioniPrimary (citable) accession number: Q80V26
Secondary accession number(s): A6H6P6
<p>This subsection of the ‘Entry information’ section shows the date of integration of the entry into UniProtKB, the date of the last sequence update and the date of the last annotation modification (‘Last modified’). The version number for both the entry and the <a href="http://www.uniprot.org/help/canonical_and_isoforms">canonical sequence</a> are also displayed.<p><a href='/help/entry_history' target='_top'>More...</a></p>Entry historyiIntegrated into UniProtKB/Swiss-Prot: May 29, 2007
Last sequence update: June 1, 2003
Last modified: May 8, 2019
This is version 129 of the entry and version 1 of the sequence. See complete history.
<p>This subsection of the ‘Entry information’ section indicates whether the entry has been manually annotated and reviewed by UniProtKB curators or not, in other words, if the entry belongs to the Swiss-Prot section of UniProtKB (<strong>reviewed</strong>) or to the computer-annotated TrEMBL section (<strong>unreviewed</strong>).<p><a href='/help/entry_status' target='_top'>More...</a></p>Entry statusiReviewed (UniProtKB/Swiss-Prot)
Annotation programChordata Protein Annotation Program

<p>This section contains any relevant information that doesn’t fit in any other defined sections<p><a href='/help/miscellaneous_section' target='_top'>More...</a></p>Miscellaneousi

Keywords - Technical termi

Complete proteome, Reference proteome

Documents

  1. SIMILARITY comments
    Index of protein domains and families
  2. MGD cross-references
    Mouse Genome Database (MGD) cross-references in UniProtKB/Swiss-Prot
  3. PATHWAY comments
    Index of metabolic and biosynthesis pathways
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